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Analysis of βB1-crystallin unfolding equilibrium by spin and fluorescence labeling: Evidence of a dimeric intermediate

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Title: Analysis of βB1-crystallin unfolding equilibrium by spin and fluorescence labeling: Evidence of a dimeric intermediate
Authors: Koteiche, Hanane A.1, Kumar, M. Satish1, Mchaourab, Hassane S. hassane.mchaourab@vanderbilt.edu
Source: FEBS Letters. May2007, Vol. 581 Issue 10, p1933-1938. 6p.
Subjects: Electron paramagnetic resonance, Particles (Nuclear physics), Magnetic resonance, Radioactivity
Abstract: Abstract: A central step in understanding lens aging is to characterize the thermodynamic stability of its proteins and determine the consequences of changes in the primary sequence on their folding equilibria. For this purpose, destabilized mutations were introduced in βB1-crystallin targeting the domain interface within the fold of a subunit. Global unfolding was monitored by tryptophan fluorescence while concomitant structural changes at the dimer interface were monitored by fluorescence and spin labels. Both spectral probes report explicit evidence of multi-state unfolding equilibrium. The biphasic nature of the unfolding curves was more pronounced at higher protein concentration. Distinct shifts in the midpoint of the second transition reflect the population of a dimeric intermediate. This intermediate may be a critical determinant for the life-long stability of the β-crystallins and has important consequences on interactions with α-crystallin. [Copyright &y& Elsevier]
Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Analysis of βB1-crystallin unfolding equilibrium by spin and fluorescence labeling: Evidence of a dimeric intermediate
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  Data: <searchLink fieldCode="AR" term="%22Koteiche%2C+Hanane+A%2E%22">Koteiche, Hanane A.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Kumar%2C+M%2E+Satish%22">Kumar, M. Satish</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Mchaourab%2C+Hassane+S%2E%22">Mchaourab, Hassane S.</searchLink><i> hassane.mchaourab@vanderbilt.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. May2007, Vol. 581 Issue 10, p1933-1938. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Electron+paramagnetic+resonance%22">Electron paramagnetic resonance</searchLink><br /><searchLink fieldCode="DE" term="%22Particles+%28Nuclear+physics%29%22">Particles (Nuclear physics)</searchLink><br /><searchLink fieldCode="DE" term="%22Magnetic+resonance%22">Magnetic resonance</searchLink><br /><searchLink fieldCode="DE" term="%22Radioactivity%22">Radioactivity</searchLink>
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  Data: Abstract: A central step in understanding lens aging is to characterize the thermodynamic stability of its proteins and determine the consequences of changes in the primary sequence on their folding equilibria. For this purpose, destabilized mutations were introduced in βB1-crystallin targeting the domain interface within the fold of a subunit. Global unfolding was monitored by tryptophan fluorescence while concomitant structural changes at the dimer interface were monitored by fluorescence and spin labels. Both spectral probes report explicit evidence of multi-state unfolding equilibrium. The biphasic nature of the unfolding curves was more pronounced at higher protein concentration. Distinct shifts in the midpoint of the second transition reflect the population of a dimeric intermediate. This intermediate may be a critical determinant for the life-long stability of the β-crystallins and has important consequences on interactions with α-crystallin. [Copyright &y& Elsevier]
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  Data: <i>Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.febslet.2007.04.004
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        Text: English
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        PageCount: 6
        StartPage: 1933
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        Type: general
      – SubjectFull: Particles (Nuclear physics)
        Type: general
      – SubjectFull: Magnetic resonance
        Type: general
      – SubjectFull: Radioactivity
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      – TitleFull: Analysis of βB1-crystallin unfolding equilibrium by spin and fluorescence labeling: Evidence of a dimeric intermediate
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              Text: May2007
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